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Related Concept Videos

Channel Rhodopsins01:11

Channel Rhodopsins

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Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
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G-Protein Gated Ion Channels01:21

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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category,...
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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Related Experiment Video

Updated: Aug 20, 2025

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
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Physiological changes in bilayer thickness induced by cholesterol control GPCR rhodopsin function.

Olivier Soubias1, Alexander J Sodt2, Walter E Teague3

  • 1Macromolecular NMR Section, Center for Structural Biology, Center for Cancer Research, NCI, NIH, Frederick, Maryland.

Biophysical Journal
|November 24, 2022
PubMed
Summary

Cholesterol

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Area of Science:

  • Biophysics
  • Membrane Biology
  • Structural Biology

Background:

  • G-protein-coupled receptors (GPCRs) are crucial membrane proteins.
  • Rhodopsin serves as a model for studying GPCR function.
  • Bilayer properties significantly influence receptor activity.

Purpose of the Study:

  • To investigate how cholesterol-induced changes in bilayer thickness affect rhodopsin function.
  • To elucidate the relationship between membrane mechanics and GPCR equilibrium.
  • To understand the role of elastic deformations in protein function.

Main Methods:

  • UV-visible spectroscopy to monitor the metarhodopsin-I (MI)/metarhodopsin-II (MII) equilibrium.
  • Deuterium nuclear magnetic resonance (2H-NMR) to probe hydrocarbon chain ordering.
  • Utilizing phosphatidylcholine bilayers with varying hydrophobic thicknesses (21-38 Å).

Main Results:

  • Cholesterol shifted the MI/MII equilibrium towards MII in thinner bilayers (<27 Å) and towards MI in thicker bilayers (>27 Å).
  • Small changes in bilayer thickness near the protein's hydrophobic length caused significant regulation of MII formation.
  • Cholesterol-induced shifts correlated with increased bilayer thickness and rhodopsin oligomerization in thicker membranes.

Conclusions:

  • Bilayer mechanical properties, modulated by cholesterol, critically influence the functional equilibrium of rhodopsin.
  • Elastic deformations around the protein are a major energetic factor in GPCR functional states.
  • Understanding these lipid-protein interactions is key to deciphering GPCR regulation in physiological membranes.